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Alkane production from fatty alcohols by the combined reactions catalyzed by an alcohol dehydrogenase and an aldehyde-deformylating oxygenase

ABSTRACT PsADH, an alcohol dehydrogenase originating in Pantoea sp. was characterized and found to convert a broad variety of fatty alcohols into their corresponding aldehydes, the substrates of alkane biosynthesis. By coupling PsADH with NpAD, a cyanobacterial aldehyde-deformylating oxygenase, and...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2023-07, Vol.87 (8), p.925-932
Main Authors: Sui, Yu-An, Maruyama, Satoshi, Okada, Natsumi, Ito, Masakazu, Muramatsu, Masayoshi, Obata, Shusei, Ogawa, Jun, Kishino, Shigenobu
Format: Article
Language:English
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Summary:ABSTRACT PsADH, an alcohol dehydrogenase originating in Pantoea sp. was characterized and found to convert a broad variety of fatty alcohols into their corresponding aldehydes, the substrates of alkane biosynthesis. By coupling PsADH with NpAD, a cyanobacterial aldehyde-deformylating oxygenase, and by optimizing the conditions of the enzyme-catalyzed reactions, we achieved a 52% conversion of 1-tetradecanol to tridecane. We further applied this system to generate alkanes ranging from C5–17. These alkanes can be used as biofuels, suggesting that introducing a suitable alcohol dehydrogenase is an effective strategy to utilize fatty alcohols for alkane production. Graphical Abstract Graphical Abstract By combining reactions catalyzed by an alcohol dehydrogenase and an aldehyde-deformylating oxygenase, we constructed an alkane biosynthesis process from fatty alcohols in Escherichia coli.
ISSN:1347-6947
1347-6947
DOI:10.1093/bbb/zbad056